Mutational and crystallographic analyses of the active site residues of the bacillus circulans xylanase. Determined by X-ray diffraction at 1.81 Å resolution. Released 15 Oct 1994.
Explore 1BCX in 3D Show helices and sheets RCSB PDB PDBe
1BCX contains 3 α-helices and 13 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 1 |
| β-strand | 15-20 | 6 | 2 |
| β-strand | 25-31 | 7 | 2 |
| β-strand | 35-42 | 8 | 1 |
| β-strand | 50-61 | 12 | 2 |
| β-strand | 64-73 | 10 | 1 |
| β-strand | 77-85 | 9 | 1 |
| β-strand | 93-100 | 8 | 1 |
| β-strand | 103-116 | 14 | 1 |
| β-strand | 122-132 | 11 | 1 |
| α-helix | 135-137 | 3 | |
| β-strand | 142-145 | 4 | 2 |
| α-helix | 146-155 | 10 | |
| α-helix | 159-161 | 3 | |
| β-strand | 163-174 | 12 | 1 |
| β-strand | 177-184 | 8 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Xylanase | A | protein | 185 | Bacillus circulans | P09850 (AlphaFold model) |
>1BCX_1 XYLANASE (chains A) ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAGVWAP NGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKSDGGTYDIYTTTRYNAPSIDG DRTTFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGSNWAYQVMATCGYQSSGSS NVTVW
Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase. Wakarchuk, W.W., Campbell, R.L., Sung, W.L. et al. Protein Sci (1994) 3:467-475. PubMed
Other PDB entries of the same protein (UniProt P09850 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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